(Q54601480)

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Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants.

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

protein folding

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molecular chaperones

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1 reference

based on heuristic

inferred from title

author name string

Li Y

1

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

Hu Z

2

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

Jordan F

3

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

Inouye M

4

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

language of work or name

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publication date

1 October 1995

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

270

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

42

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

25127-25132

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

A protein-folding reaction under kinetic control

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Protease pro region required for folding is a potent inhibitor of the mature enzyme.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

A covalently trapped folding intermediate of subtilisin E: spontaneous dimerization of a prosubtilisin E Ser49Cys mutant in vivo and its autoprocessing in vitro.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Pro-subtilisin E: purification and characterization of its autoprocessing to active subtilisin E in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Intramolecular chaperones and protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Folding mediated by an intramolecular chaperone: autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Folding pathway mediated by an intramolecular chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Use of T7 RNA polymerase to direct expression of cloned genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Tight-binding inhibitors-I. Kinetic behavior

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Potent slow-binding inhibition of cathepsin B by its propeptide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Functional analysis of the intramolecular chaperone. Mutational hot spots in the subtilisin pro-peptide and a second-site suppressor mutation within the subtilisin molecule

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected]

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.42.25127

21 January 2018

Identifiers

10.1074/JBC.270.42.25127

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7559646

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